SYR_CORGB
ID SYR_CORGB Reviewed; 550 AA.
AC A4QDE1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Arginine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00123};
DE EC=6.1.1.19 {ECO:0000255|HAMAP-Rule:MF_00123};
DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00123};
DE Short=ArgRS {ECO:0000255|HAMAP-Rule:MF_00123};
GN Name=argS {ECO:0000255|HAMAP-Rule:MF_00123}; OrderedLocusNames=cgR_1259;
OS Corynebacterium glutamicum (strain R).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=340322;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R;
RX PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT "Comparative analysis of the Corynebacterium glutamicum group and complete
RT genome sequence of strain R.";
RL Microbiology 153:1042-1058(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-
CC tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA-
CC COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215;
CC EC=6.1.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_00123};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00123}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00123}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00123}.
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DR EMBL; AP009044; BAF54238.1; -; Genomic_DNA.
DR RefSeq; WP_011897085.1; NC_009342.1.
DR AlphaFoldDB; A4QDE1; -.
DR SMR; A4QDE1; -.
DR EnsemblBacteria; BAF54238; BAF54238; cgR_1259.
DR KEGG; cgt:cgR_1259; -.
DR HOGENOM; CLU_006406_0_1_11; -.
DR OMA; NKPLHLG; -.
DR PhylomeDB; A4QDE1; -.
DR Proteomes; UP000006698; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00671; ArgRS_core; 1.
DR Gene3D; 3.30.1360.70; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00123; Arg_tRNA_synth; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR001278; Arg-tRNA-ligase.
DR InterPro; IPR005148; Arg-tRNA-synth_N.
DR InterPro; IPR036695; Arg-tRNA-synth_N_sf.
DR InterPro; IPR035684; ArgRS_core.
DR InterPro; IPR008909; DALR_anticod-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR PANTHER; PTHR11956; PTHR11956; 1.
DR Pfam; PF03485; Arg_tRNA_synt_N; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF00750; tRNA-synt_1d; 1.
DR PRINTS; PR01038; TRNASYNTHARG.
DR SMART; SM01016; Arg_tRNA_synt_N; 1.
DR SMART; SM00836; DALR_1; 1.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF55190; SSF55190; 1.
DR TIGRFAMs; TIGR00456; argS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..550
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000018019"
FT MOTIF 130..140
FT /note="'HIGH' region"
SQ SEQUENCE 550 AA; 59681 MW; 21F724BDE9E3532F CRC64;
MTPADLATLI KETAVEVLTS RELDTSVLPE QVVVERPRNP EHGDYATNIA LQVAKKVGQN
PRDLATWLAE ALAADDAIDS AEIAGPGFLN IRLAAAAQGE IVAKILAQGE TFGNSDHLSH
LDVNLEFVSA NPTGPIHLGG TRWAAVGDSL GRVLEASGAK VTREYYFNDH GRQIDRFALS
LLAAAKGEPT PEDGYGGEYI KEIAEAIVEK HPEALALEPA ATQELFRAEG VEMMFEHIKS
SLHEFGTDFD VYYHENSLFE SGAVDKAVQV LKDNGNLYEN EGAWWLRSTE FGDDKDRVVI
KSDGDAAYIA GDIAYVADKF SRGHNLNIYM LGADHHGYIA RLKAAAAALG YKPEGVEVLI
GQMVNLLRDG KAVRMSKRAG TVVTLDDLVE AIGIDAARYS LIRSSVDSSL DIDLGLWESQ
SSDNPVYYVQ YGHARLCSIA RKAETLGVTE EGADLSLLTH DREGDLIRTL GEFPAVVKAA
ADLREPHRIA RYAEELAGTF HRFYDSCHIL PKADEDTAPI HSARLALAAA TRQTLANALH
LVGVSAPEKM